But health officials said this elderly man's illness has not been linked to eating tainted beef or deer. Privacy laws prohibit naming the man.

"This is a different form with a different cause," said Dr. Julie Sinclair, the Epidemic Intelligence Officer assigned to the state Bureau of Public Health by the Centers for Disease Control and Prevention. "There is an undetermined cause in this guy. They are doing further investigation."

Dr. John Schmidt, who performed a brain biopsy and another procedure on the patient, said this would be his first CJD case in 25 years of doing neurosurgery.

"This is a big deal," Schmidt said. "You have a diagnosis of CJD. It's really weird -- not from a virus, not a bacterium and uniformly fatal. It takes a long time to develop."

Hospital safety officers had to take special precautions for the surgery, from removing all extraneous equipment from the operating room to quarantining the surgical instruments. If specialized lab work confirms a definitive diagnosis of CJD, then the instruments would have to be destroyed, Schmidt said.

And all medical waste collected had to be immediately incinerated, said CAMC spokesman Dale Witte.

Though no cases of iatrogenic (caused by medical treatment) CJD have been reported since current sterilization procedures were adopted in 1976, transmission of CJD occurred in at least 250 patients worldwide, according to the CDC. These were linked to contaminated human growth hormone, corneal grafts or surgical equipment.

Schmidt said he knows of one case of a brain surgeon infected with CJD after he operated on a patient with it.

Still, CJD is extremely rare, happening in only one in a million people, Sinclair said. Most cases are confirmed through a post-mortem exam.

Since 1979, 31 deaths have been attributed to CJD in West Virginia, Sinclair said. All the victims were older than 40 and most were over 60.

Most cases occur sporadically. That means no recognizable pattern of transmission exists.

Meanwhile, the Centers for Disease Control is quietly reviewing several mysterious deaths of young Americans from CJD to discern if they may have eaten cows with the disease. Deaths have occurred over the last five years in several states, including New Jersey, Texas, Michigan and Wisconsin, according to the Associated Press.

A small percentage of patients develop CJD because they inherited mutations of a protein gene called a prion.

Hospital tests manfor brain illness

Therese Smith Cox Daily Mail staff

Wednesday March 02, 2005

(Page 2 of 2)

But whatever the cause, people with the disease usually die within a year from what is classified as transmissible spongiform encephalopathy. Medical officials declined to comment on the prognosis of the man treated at CAMC.

While the disease is limited among animals, it is not uncommon, said state Agriculture Commissioner Gus Douglass.

"Mad cow disease, scrapie in sheep and chronic wasting in deer are all from the same family," he said. "We know these are transmittable to humans. Others, medical science has not proven they are transmittable. I'm not surprised we might find CJD in West Virginia."

However, the state has never had a case of mad cow disease, Douglass said.

Indeed, it has never been determined that a mad cow case has originated in the United States, he said.

Sinclair said the bureau received the report of the CJD case from a physician treating the elderly patient.

"This is a very good physician, on the ball," Sinclair said, noting that because the condition is so rare, it would be difficult to diagnose.

Sinclair also said it has not been shown that CJD could be transmitted casually from person to person.

"Family members don't have to be concerned," Sinclair said.

Contact Therese Smith Cox at 348-4874.

http://www.dailymail.com/news/News/2005030214/

http://www.dailymail.com/news/News/2005030214/?pt=15

> But health officials said this elderly man's illness has not been > linked to eating tainted beef or deer. Privacy laws prohibit naming > the man.>

RIGHT, famous last words. no proof what so ever, they refuse toacknowledge recent science of the new TSE in cattle that is veryvery similar to sporadic CJD not the nvCJD that BSE causes.this new TSE in cattle called BASE, most media is ignorant of...TSS

> "This is a different form with a different cause," said Dr. Julie > Sinclair, the Epidemic Intelligence Officer assigned to the state > Bureau of Public Health by the Centers for Disease Control and > Prevention. "There is an undetermined cause in this guy. They are > doing further investigation.">

Medical SciencesIdentification of a second bovine amyloidotic spongiformencephalopathy: Molecular similarities with sporadicCreutzfeldt-Jakob disease

Edited by Stanley B. Prusiner, University of California, San Francisco, CA, and approved December 23, 2003 (received for review September 9, 2003)

Transmissible spongiform encephalopathies (TSEs), or prion diseases, are mammalian neurodegenerative disorders characterized by a posttranslational conversion and brain accumulation of an insoluble, protease-resistant isoform (PrPSc) of the host-encoded cellular prion protein (PrPC). Human and animal TSE agents exist as different phenotypes that can be biochemically differentiated on the basis of the molecular mass of the protease-resistant PrPSc fragments and the degree of glycosylation. Epidemiological, molecular, and transmission studies strongly suggest that the single strain of agent responsible for bovine spongiform encephalopathy (BSE) has infected humans, causing variant Creutzfeldt-Jakob disease. The unprecedented biological properties of the BSE agent, which circumvents the so-called "species barrier" between cattle and humans and adapts to different mammalian species, has raised considerable concern for human health. To date, it is unknown whether more than one strain might be responsible for cattle TSE or whether the BSE agent undergoes phenotypic variation after natural transmission. Here we provide evidence of a second cattle TSE. The disorder was pathologically characterized by the presence of PrP-immunopositive amyloid plaques, as opposed to the lack of amyloid deposition in typical BSE cases, and by a different pattern of regional distribution and topology of brain PrPSc accumulation. In addition, Western blot analysis showed a PrPSc type with predominance of the low molecular mass glycoform and a protease-resistant fragment of lower molecular mass than BSE-PrPSc. Strikingly, the molecular signature of this previously undescribed bovine PrPSc was similar to that encountered in a distinct subtype of sporadic Creutzfeldt-Jakob disease.

Distinct prion strains can be distinguished by differences in incubation period, neuropathology and biochemical properties of disease-associated prion protein (PrPSc) in inoculated mice. Reliable comparisons of mouse prion strain properties can only be achieved after passage in genetically identical mice, as host prion protein sequence and genetic background are known to modulate prion disease phenotypes. While multiple prion strains have been identified in sheep scrapie and Creutzfeldt–Jakob disease, bovine spongiform encephalopathy (BSE) is thought to be caused by a single prion strain. Primary passage of BSE prions to different lines of inbred mice resulted in the propagation of two distinct PrPSc types, suggesting that two prion strains may have been isolated. To investigate this further, these isolates were subpassaged in a single line of inbred mice (SJL) and it was confirmed that two distinct prion strains had been identified. MRC1 was characterized by a short incubation time (110±3 days), a mono-glycosylated-dominant PrPSc type and a generalized diffuse pattern of PrP-immunoreactive deposits, while MRC2 displayed a much longer incubation time (155±1 days), a di-glycosylated-dominant PrPSc type and a distinct pattern of PrP-immunoreactive deposits and neuronal loss. These data indicate a crucial involvement of the host genome in modulating prion strain selection and propagation in mice. It is possible that multiple disease phenotypes may also be possible in BSE prion infection in humans and other animals.

There is substantial scientific evidence to support the notion that bovine spongiform encephalopathy (BSE) has contaminated human beings, causing variant Creutzfeldt-Jakob disease (vCJD). This disease has raised concerns about the possibility of an iatrogenic secondary transmission to humans, because the biological properties of the primate-adapted BSE agent are unknown. We show that (i) BSE can be transmitted from primate to primate by intravenous route in 25 months, and (ii) an iatrogenic transmission of vCJD to humans could be readily recognized pathologically, whether it occurs by the central or peripheral route. Strain typing in mice demonstrates that the BSE agent adapts to macaques in the same way as it does to humans and confirms that the BSE agent is responsible for vCJD not only in the United Kingdom but also in France. The agent responsible for French iatrogenic growth hormone-linked CJD taken as a control is very different from vCJD but is similar to that found in one case of sporadic CJD and one sheep scrapie isolate. These data will be key in identifying the origin of human cases of prion disease, including accidental vCJD transmission, and could provide bases for vCJD risk assessment.

snip...

ConclusionsTop Abstract Introduction

Materials and Methods

Results Discussion ConclusionsReferences

From BSE and vCJD transmissions in nonhuman primates, a number of conclusions can be drawn that are of major importance for human health: (i) human-adapted BSE appears to be a variant of the BSE agent that is more virulent for humans than cattle BSE and is efficiently transmitted by the peripheral route; (ii) the detection of vCJD in unusually young patients is probably not because of a lack of diagnosis of cases in older patients, thus raising the question of the source of human contamination with BSE early in life; and (iii) iatrogenic transmissions from patients with vCJD would be readily recognized by using the same diagnostic criteria as those applied to vCJD [clinical and pathological criteria (27 ) comprising neuronal loss and gliosis in the thalamus correlated with high MRI signal (28 , 29 )], whether such contaminations had occurred by the central or i.v. route. Primary and iatrogenic cases of vCJD could be distinguished on the basis of the patient's clinical history.

The risk assessment of biological products of human origin, notably those derived from blood, has been deeply modified by the appearance of vCJD. We confirm that the BSE agent has contaminated humans not only in the U.K. and the Republic of Ireland but also in France, and we show that its pathogenic properties for primates are being enhanced by a primary passage in humans. Considering the flow of potentially contaminated bovine-derived products between 1980 and 1996, it is obvious that further vCJD cases may occur outside the U.K. Thus, and in the light of the present study, it is necessary to sustain worldwide CJD surveillance regardless of national BSE incidence and to take all precautionary measures to avoid iatrogenic transmissions from vCJD.

snip...

full text;

http://www.pnas.org/cgi/content/full/041490898v1

Ref: MRC/62/04

Under strict embargo until 19.00 British Time Thursday 11 November 2004

GENETIC MAKE-UP MAY DETERMINE WHAT TYPE OF CJD OCCURS WHEN HUMANS ARE

INFECTED WITH BSE

New research published today (19.00 hours Thursday 11th November) by a

team from the Medical Research Council (MRC) Prion Unit offers an

explanation about why only people with a particular genetic make-up have

so far developed vCJD. It also provides evidence that other types of

BSE-derived prion infection with a different pattern of symptoms might

occur in humans. The findings are published in the journal Science.

Variant CJD (vCJD) is the human disease thought to be caused by eating

food contaminated with the infectious agent, known as a prion,

responsible for the epidemic of BSE or mad cow disease in cattle. So

far, everyone known to have developed vCJD has been of a particular

genetic type known as MM. Until now it has been a mystery why everyone

that has developed vCJD is of the MM type and one possibility is that

they are simply the first to develop the disease when infected with BSE,

and that people with the other genetic types1 (known as VV and MV)

infected with BSE prions will also develop vCJD, but some years later.

In a series of experiments spanning more than ten years, the MRC team

has been studying mice genetically modified so that they make human

prion proteins which are used to model human susceptibility to BSE.

The team has now shown that mice with the human VV genetic type do

become infected when given BSE or vCJD prions, but manifest a different

form of the disease which looks quite different to vCJD and has a novel

prion strain type.

Remarkably, when these novel prions were used to infect mice of the MM

genetic type, the mice either developed a disease very like vCJD, or

else a pattern of disease that looks like so-called sporadic CJD the

classical form of CJD. This form has been known about for many years,

is seen all over the world and has not hitherto been associated with

BSE. However, the new strain identified in the mice, being called type

5, has not been seen yet in people and we do not know what pattern of

disease it would cause. It could look like one of the forms of classical

or sporadic CJD or perhaps be yet another different variant form.

The work from the MRC team suggests that type 4 prions, the type

associated with vCJD, can only propagate themselves in people that make